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Literature summary for 2.7.11.19 extracted from

  • Rimmer, M.A.; Artigues, A.; Nadeau, O.W.; Villar, M.T.; Vasquez-Montes, V.; Carlson, G.M.
    Mass spectrometric analysis of surface-exposed regions in the hexadecameric phosphorylase kinase complex (2015), Biochemistry, 54, 6887-6895.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin required Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
additional information loss of activity through proteolysis only by ficin digestion Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ dependent on Oryctolagus cuniculus
Mg2+ required Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
16700
-
-
Oryctolagus cuniculus
44700
-
-
Oryctolagus cuniculus
125200
-
-
Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Oryctolagus cuniculus the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme ?
-
?
additional information Oryctolagus cuniculus New Zealand White the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme ?
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P18688 AND P12798 subunits alpha and beta
-
Oryctolagus cuniculus New Zealand White P18688 AND P12798 subunits alpha and beta
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information loss of activity through proteolysis only by ficin digestion Oryctolagus cuniculus
phosphoprotein when PhK is phosphorylated, the alpha subunit is cleaved in the same loop regions (656-748 and 967-1015). A new region (627-662) proximal to the former loop is observed. Additionally, two new regions near the C-terminus of alpha appear, as well as a peptide corresponding to residues 1103-1113 and one of residues 1217-1224. Cys1234 is modified only in the phosphorylated complex. The entire C-terminus from residues 1217 to 1237 may be more exposed in the activated conformer Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
psoas
-
Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme Oryctolagus cuniculus ?
-
?
additional information the alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme Oryctolagus cuniculus New Zealand White ?
-
?

Subunits

Subunits Comment Organism
hexadecamer (alphabetagammadelta)4 , 4 x 138400, alpha-subunit, + 4 * 125200, beta-subunit, + 4 * 44700, gamma-subunit, + 4 * 16700, delta-subunit, about, mass spectrometry Oryctolagus cuniculus
More mass spectrometric analysis of surface-exposed regions in the hexadecameric phosphorylase kinase complex, overview. Phosphorylase kinase is a 1.3 MDa (alphabetagammadelta)4 enzyme complex, in which alphabetagammadelta protomers associate in D2 symmetry to form two large octameric lobes that are interconnected by four bridges. The alpha, beta, and delta subunits are regulatory, inhibiting the kinase activity of the catalytic gamma subunit until beta and then alpha are phosphorylated by protein kinase A which releases the inhibition and allows gamma to phosphorylate glycogen phosphorylase in a Ca2+-dependent reaction. The delta subunit is an intrinsic calmodulin molecule, which accounts for the Ca2+ sensitivity of the enzyme. Enzyme structure analysis by mass spectrometry, small-angle X-ray scattering, and transmission electron microscopy Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
PhK
-
Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
assay at Oryctolagus cuniculus